title: The use of proteolysis and direct N-terminal sequence analysis to study human interleukin-2/receptor interaction on solid support.
abstract: An immobilized interleukin-2 receptor which is capable of binding interleukin-2 and suitable for direct N-terminal sequence analysis was employed to study interleukin-2/receptor interactions. Sensitive tryptic sites on the immobilized receptor and its interleukin-2 complex were identified by sequence analyses and compared. The results have revealed that the N-terminal region of interleukin-2 is not involved in receptor binding and the peptide segment covering residues 36-39 in the receptor is probably near or involved in the interleukin-2 binding site. The rapidity and simplicity make this solid phase sequence approach a good method for analyzing interleukin-2/receptor interaction and may be suitable for studying other protein-ligand interactions.
authors.affiliation: Department of Protein Biochemistry, Hoffmann-La Roche Inc., Nutley, NJ.
authors.forename: Y C
authors.initials: YC
authors.lastname: Pan
authors.forename: F
authors.initials: F
authors.lastname: Wang
authors.forename: M C
authors.initials: MC
authors.lastname: Miedel
authors.forename: D V
authors.initials: DV
authors.lastname: Weber
authors.forename: P
authors.initials: P
authors.lastname: Bailon
authors.forename: F R
authors.initials: FR
authors.lastname: Khan
authors.forename: J D
authors.initials: JD
authors.lastname: Hulmes
mesh_terms: D000595:Amino Acid Sequence; D002846:Chromatography, Affinity / Q000379:methods; D006801:Humans; D007376:Interleukin-2 / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D015375:Receptors, Interleukin-2 / Q000378:metabolism*; D014357:Trypsin
chemical_list: D007376:Interleukin-2; D010446:Peptide Fragments; D015375:Receptors, Interleukin-2; D014357:Trypsin